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NU5C_VICFA
ID   NU5C_VICFA              Reviewed;         746 AA.
AC   P15958;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase subunit 5;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 5;
GN   Name=ndhF;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2320425; DOI=10.1093/nar/18.5.1297;
RA   Herdenberger F., Pillay D.T.N., Steinmetz A.;
RT   "Sequence of the trnH gene and the inverted repeat structure deletion site
RT   of the broad bean chloroplast genome.";
RL   Nucleic Acids Res. 18:1297-1297(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3242868; DOI=10.1007/bf00434087;
RA   Herdenberger F., Weil J.H., Steinmetz A.;
RT   "Organization and nucleotide sequence of the broad bean chloroplast genes
RT   trnL-UAG, ndhF and two unidentified open reading frames.";
RL   Curr. Genet. 14:609-615(1988).
CC   -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC       and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC       and possibly in a chloroplast respiratory chain. The immediate electron
CC       acceptor for the enzyme in this species is believed to be
CC       plastoquinone. Couples the redox reaction to proton translocation, and
CC       thus conserves the redox energy in a proton gradient (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; X51471; CAA35834.1; -; Genomic_DNA.
DR   EMBL; X14804; CAA32909.1; -; Genomic_DNA.
DR   EMBL; M36832; AAA84714.1; -; Genomic_DNA.
DR   PIR; S08494; S08494.
DR   AlphaFoldDB; P15958; -.
DR   SMR; P15958; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; PTHR42829; 1.
DR   Pfam; PF01010; Proton_antipo_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..746
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT                   chloroplastic"
FT                   /id="PRO_0000118207"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        552..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        606..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        726..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   746 AA;  84768 MW;  252471990B47CF9C CRC64;
     MEYTHQSSWI IPFIPLPVPI LIGVGLLLFP TATKNLRRMW AFPSIFLLTI VMIFSIDLSI
     QQIENSSIYQ YVWSWTINND LSLEFGYLID SLTSIMSILI TTVGILVLIY SDSYMSHDQG
     YLRFFTYMSF FNTSMLGLVT SSNLIQVYIF WELVGMCSYL LIGFWFTRPI AANACQKAFV
     TNRVGDFGLL LGILGFYWIT GSLEFRDLFQ IFKNLIYKNE VNILFVTLCA LLLFCGSVAK
     SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPSI MSGIALIGII
     TVVLGATLAI AQKDIKKNLA YSTMSQLGYM MLALGMGSYR AALFHLITHA YSKALLFLGS
     GSIIHSMEAI VGYSPDKSQN MVLMGGLTKH APITKMSFLI GTLSLCGIPP FACFWSKDEI
     LNDSWLYSPI FAIIACSTAG LTAFYMFRIY LLVFEGYLNV HFQNFNGKKN SSFYSISLWG
     KEEKKKLKKK IHLLGFLTMN NNERTSFFRE RTYSHRINRN VKSIRRLFLD STHFGTKNLP
     FFYPHESDNT MLFSMLVLVL FTFFVGSIGI SFSQEGIDLD ILSKLLIPSI DLLHQNSKNS
     VDWYEFFINA TFSVSIAFFG LFIASFFYKP VFSSLQNLNL FNLFQKNVPK KIISDKIINI
     LYDWSYNRGY IDAFFEVSLI ASVRKLAKFN YFFDRQLIDG IPNGVGISNF FIGEAIKYVG
     GGRISSYIFF FVLIFLLICY YIYLFP
 
 
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